(Q48314402)

10 February 2018

title

Functional domains on chemically modified tau protein. (English)

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10 February 2018

author name string

G A Farías

series ordinal

1

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10 February 2018

C Vial

series ordinal

2

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10 February 2018

R B Maccioni

series ordinal

3

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10 February 2018

publication date

1 April 1993

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10 February 2018

Cellular and Molecular Neurobiology

published in

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10 February 2018

volume

13

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10 February 2018

issue

2

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10 February 2018

page(s)

173-182

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10 February 2018

https://scigraph.springernature.com/pub.10.1007/bf00735373

exact match

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cites work

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Phosphorylation affects the ability of tau protein to promote microtubule assembly.

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Fractionation of brain microtubule-associated proteins. Isolation of two different proteins which stimulate tubulin polymerization in vitro

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Neurofibrillary tangles of Alzheimer disease share antigenic determinants with the axonal microtubule-associated protein tau (tau)

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MAP-1 and MAP-2 binding sites at the C-terminus of beta-tubulin. Studies with synthetic tubulin peptides.

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Microtubule-associated protein tau. Identification of a novel peptide from bovine brain.

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A68: a major subunit of paired helical filaments and derivatized forms of normal Tau.

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Tubulin carbamoylation. Functional amino groups in microtubule assembly

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Tau proteins: the molecular structure and mode of binding on microtubules

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The microtubule-associated protein tau forms a triple-stranded left-hand helical polymer

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Phosphate-dependent monoclonal antibodies to neurofilaments and Alzheimer neurofibrillary tangles recognize a synthetic phosphopeptide

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Heat-stable microtubule protein MAP-1 binds to microtubules and induces microtubule assembly

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Specific macromolecular interactions between tau and the microtubule system.

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Alzheimer's neurofibrillary tangles contain unique epitopes and epitopes in common with the heat-stable microtubule associated proteins tau and MAP2.

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12 December 2020

Defective brain microtubule assembly in Alzheimer's disease

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Phosphorylation of microtubule-associated proteins regulates their interaction with actin filaments

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Phosphorylation of Tau proteins: a major event during the process of neurofibrillary degeneration. A comparative study between Alzheimer's disease and Down's syndrome.

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Tau proteins of Alzheimer paired helical filaments: abnormal phosphorylation of all six brain isoforms

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The primary structure and heterogeneity of tau protein from mouse brain.

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Tau protein function in living cells

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Expression of multiple tau isoforms and microtubule bundle formation in fibroblasts transfected with a single tau cDNA.

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Subunit structure of paired helical filaments in Alzheimer's disease

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The microtubule binding domain of tau protein.

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12 December 2020

Abnormal tau proteins from Alzheimer's disease brains. Purification and amino acid analysis.

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Isolation of a fragment of tau derived from the core of the paired helical filament of Alzheimer disease

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12 December 2020

In vitro conditions for the self-polymerization of the microtubule-associated protein, tau factor

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A preparation of Alzheimer paired helical filaments that displays distinct tau proteins by polyacrylamide gel electrophoresis

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12 December 2020

A discrete repeated sequence defines a tubulin binding domain on microtubule-associated protein tau.

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12 December 2020

Accumulation of abnormally phosphorylated tau precedes the formation of neurofibrillary tangles in Alzheimer's disease

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Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease

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12 December 2020

Differential interaction of synthetic peptides from the carboxyl-terminal regulatory domain of tubulin with microtubule-associated proteins

1 reference

12 December 2020

Phosphorylation of microtubule-associated protein tau: identification of the site for Ca2(+)-calmodulin dependent kinase and relationship with tau phosphorylation in Alzheimer tangles.

1 reference

12 December 2020

Identifiers

DOI

10.1007/BF00735373

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10 February 2018

PubMed ID

8348591

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10 February 2018